Results 101 to 110 of about 1,955 (147)
Exploration of Antiplasmodium Chemical Space Identifies New Inhibitors of β-Hematin Formation from Areas of Enrichment. [PDF]
ChemMedChemThibaud JL +9 more
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Hemeproteins as Targets for Sulfide Species
Antioxidants and Redox Signaling, 2020Significance: Sulfides are endogenous and ubiquitous signaling species that share the hemeproteins as biochemical targets with O 2 , nitric oxide, and carbon monoxide.
Darío A. Estrin +2 more
exaly +4 more sources
How does NO activate hemeproteins? [PDF]
FEBS Letters, 1994 NO was reported to activate guanylate cyclase and, recently, prostaglandin H synthase. NO interaction with the heme component in different hemeproteins is determined by ligand property, electronic configuration of the heme iron and the specific effects contributed by the protein structure.
Ah-Lim Tsai
exaly +3 more sources
Oxidative modification of quercetin by hemeproteins
Biochemical and Biophysical Research Communications, 2006The ability of a number of hemeproteins to oxidize the flavonoid quercetin has been shown. It was found that quercetin undergoes chemical modification in the presence of cytochrome c, myoglobin, and hemoglobin but not cytochrome b(5). In the range of investigated proteins the most effective oxidant appears to be cytochrome c.
Alexander V Baranovsky +2 more
exaly +3 more sources
Journal of Chemical Sciences, 1995
Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region.
Tapan K Das +2 more
exaly +2 more sources
Structural change due to acid-alkaline transition in hemeproteins were monitored by circular dichroism measurements in the Soret region. It was observed that in cytochrome c and horseradish peroxidase, alkaline transition results in a large change in the heme CD due to significant conformational change in the heme cavity region.
Tapan K Das +2 more
exaly +2 more sources
On the biosynthesis of heme and hemeproteins in liver cell
Biochimica Et Biophysica Acta, 1958Haruhisa Yoshikawa +2 more
exaly +3 more sources
Measurement of O2 Binding by Sensory Hemeproteins
2023The discovery of an increasing number of proteins that function in the detoxification and sensing of gaseous ligands has renewed interest in hemeproteins. It is critical to measure the affinities of these proteins for ligands like O2, CO, and NO, know with confidence when a protein is fully saturated with a specific ligand, and be able to estimate how ...
Marie A, Gilles-Gonzalez +1 more
openaire +2 more sources
OXIDATION‐REDUCTION REACTIONS OF HEMEPROTEINS
Annals of the New York Academy of Sciences, 1975iiiii Then on past C 1, C, and A On through copper and all the way To oxygen, with two‐faced grin Cavorting and contorting with unpaired spin ...
C E, Castro +5 more
openaire +2 more sources
2007
Hemeproteins are widespread in all groups of living organisms, both as components of key biological processes as well as in very specific metabolic pathways. By variation of either the heme porphyrin structure or the heme protein environment, the function and behavior of the hemeproteins may vary drastically, allowing its role in the most diverse ...
Inês A. C. Pereira +2 more
openaire +1 more source
Hemeproteins are widespread in all groups of living organisms, both as components of key biological processes as well as in very specific metabolic pathways. By variation of either the heme porphyrin structure or the heme protein environment, the function and behavior of the hemeproteins may vary drastically, allowing its role in the most diverse ...
Inês A. C. Pereira +2 more
openaire +1 more source